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Binding of water and electrolytes to proteins. An equilibrium dialysis study

✍ Scribed by Henry B. Bull; Keith Breese

Publisher: Wiley (John Wiley & Sons)
Year: 1976
Tongue: English
Weight: 584 KB
Volume: 15
Category: Article
ISSN: 0006-3525
DOI: 10.1002/bip.1976.360150811

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✦ Synopsis

The technique of equilibrium dialysis has been used to study water and salt binding to egg albumin, to human carbon monoxide hemoglobin, and to bovine serum albumin. The salts used were CsC1, KC1, NaCl, LiC1, Gu.HC1, NaBr, Cs2SO4, KzS04, Na2S04, Li2SO4, and Gu2S04. The amount of water bound by proteins depends on the probe being used. Sulfates tend to bind to proteins and they also increase the water binding. A t saturation, about 41 and 140 mol GwHC1 bind to 1 mol egg albumin and to 1 mol carbon monoxide hemoglobin, respectively. Both proteins are dehydrated by GwHCl.

The hydrodynamic hydration of egg albumin as determined by viscosity appears to increase as the relative viscosity of the medium increases. 14. Chothia, C. (1975) Nature 254,304-308. 2nd ed.

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